› 3a1d

X-ray diffraction
1.85Å resolution

Crystal structure of the P- and N-domains of CopA, a copper-transporting P-type ATPase, bound with ADP-Mg

Released:
DOI: 10.2210/pdb3a1d/pdb
PDB entry 3a1d coloured by chain, front view.
PDB entry 3a1d coloured by chain, side view.
PDB entry 3a1d coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase.
Tsuda T, Toyoshima C
EMBO J 28 1782-91 (2009)
PMID: 19478797

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128171 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable copper-exporting P-type ATPase Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 30.78 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O29777 (Residues: 398-673; Coverage: 34%)
Gene names: AF_0473, copA, pacS
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ADP 2 x ADP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P4322
Unit cell:
a: 89.956Å b: 89.956Å c: 190.375Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.226
Expression system: Escherichia coli

Quick links

Citations

9 review citations

P-type ATPases.
Palmgren et al. (2011)
8 more

4 mentions without citation

Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase.
Tsuda et al. (2009)
3 more